Aspartate proteases display a variety of substrate specificities, but normally they are most active in cleavage of peptide bonds:
A) on the carboxyl side of the basic amino acids.
B) on the carboxyl side of aromatic amino acids.
C) on the carboxyl side of small, neutral residues.
D) between two hydrophobic amino acid residues.
E) none of the above.

Question

Quizplus · Accepted Answer

Aspartate proteases typically cleave peptide bonds between two hydrophobic amino acid residues, as they recognize and bind to hydrophobic regions of the substrate.

Aspartate Proteases Display a Variety of Substrate Specificities, but Normally